Reviewed, UniProtKB/Swiss-Prot A9I4U2 (MRAY_BORPD)

Names and origin

Protein names

Recommended name:
    Phospho-N-acetylmuramoyl-pentapeptide-transferase
    EC=2.7.8.13
Alternative name(s):
    UDP-MurNAc-pentapeptide phosphotransferase

Gene names

Name:	mraY
Ordered Locus Names:	Bpet0694

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan By similarity.
Catalytic activity	UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP MF_00038
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00038
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 4 family. MraY subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 389	389	Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038		PRO_1000090596
Regions
	Transmembrane	21 – 41	21	Potential
	Transmembrane	71 – 91	21	Potential
	Transmembrane	97 – 117	21	Potential
	Transmembrane	134 – 154	21	Potential
	Transmembrane	167 – 187	21	Potential
	Transmembrane	190 – 210	21	Potential
	Transmembrane	222 – 242	21	Potential
	Transmembrane	259 – 279	21	Potential
	Transmembrane	286 – 306	21	Potential
	Transmembrane	311 – 331	21	Potential
	Transmembrane	366 – 386	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	A9I4U2-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 3DFA265111049F4C	FASTA	389	42,715
	10 20 30 40 50 60 MLLEIARWLS DDVRAIGVLE YITMRAVLAC ATALLIGLVA GPRVIRKLTE MKIGQAVRAY 70 80 90 100 110 120 GPESHLVKTG TPTMGGALIL IAVAISTLLW ADWTNRFVWV VLLVTFGFGW IGWMDDYRKV 130 140 150 160 170 180 VYRDPEGMPA RQKFFWQATI GLVAAVYLAF AVSAPANTEL WPLFKAWVSS GFAMPLPTRA 190 200 210 220 230 240 DLIVPFFKSV SYPLGVLGFV ALTWAVIVGT SNAVNLTDGL DGLAIMPTVM VGSALGIFAY 250 260 270 280 290 300 VVGRVDYSKY LLFPYIPGAA ELMVLCAAIA GAGLAFLWFN AYPAQVFMGD VGALALGGAL 310 320 330 340 350 360 GTIAVIVRQE IVLFIMGGVF VVETLSVMMQ VTWFKYTKRK YGQGRRIFRM APLHHHFEVG 370 380 GWKETQVVVR FWIISMMLVL IGLSTLKLR

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM902716 Genomic DNA. Translation: CAP41026.1.
RefSeq	YP_001629297.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5819507.
GenomeReviews	Gene locus Bpet0694 in contig AM902716_GR.
KEGG	bpt:Bpet0694.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	HHHFEQK.
Family and domain databases
HAMAP	MF_00038. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR018481. Glycosyl_Trfase_4_cons-reg. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
PANTHER	PTHR22926. Glyco_trans_4. 1 hit. PTHR22926:SF3. PNAcPpept_trans. 1 hit.
Pfam	PF00953. Glycos_transf_4. 1 hit. PF10555. MraY_sig1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00445. mraY. 1 hit.
PROSITE	PS01347. MRAY_1. 1 hit. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MRAY_BORPD

Accession

Primary (citable) accession number: A9I4U2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)